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Effects of conformational stability and geometry of guanidinium display on cell entry by beta-peptides.
Potocky, Terra B; Menon, Anant K; Gellman, Samuel H.
Affiliation
  • Potocky TB; Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
J Am Chem Soc ; 127(11): 3686-7, 2005 Mar 23.
Article in En | MEDLINE | ID: mdl-15771489
We have used our ability to control beta-peptide secondary structure in order to explore the effects of conformational stability and geometry of guanidinium display on cell entry. Both of these factors affect the rate and relative amount of beta-peptide accumulation in the cytoplasm and nucleus of live HeLa cells. These beta-peptides do not show significant differences in cell surface binding, implying that structure and guanidinium display are important in a later step in cell entry than initial surface binding.
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Collection: 01-internacional Database: MEDLINE Main subject: Oligopeptides / Arginine / Guanidine Limits: Humans Language: En Journal: J Am Chem Soc Year: 2005 Document type: Article Affiliation country: United States Country of publication: United States
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Oligopeptides / Arginine / Guanidine Limits: Humans Language: En Journal: J Am Chem Soc Year: 2005 Document type: Article Affiliation country: United States Country of publication: United States